ID   AFI1_YEAST              Reviewed;         893 AA.
AC   Q99222; D6W2I7; Q92274;
DT   10-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 153.
DE   RecName: Full=ARF3-interacting protein 1;
GN   Name=AFI1; OrderedLocusNames=YOR129C; ORFNames=YOR3296C;
OS   Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX   NCBI_TaxID=559292;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 96604 / S288c / FY1679;
RX   PubMed=8904341;
RX   DOI=10.1002/(sici)1097-0061(19960315)12:3<281::aid-yea904>3.0.co;2-o;
RA   Wiemann S., Rechmann S., Benes V., Voss H., Schwager C., Vlcek C.,
RA   Stegemann J., Zimmermann J., Erfle H., Paces V., Ansorge W.;
RT   "Sequencing and analysis of 51 kb on the right arm of chromosome XV from
RT   Saccharomyces cerevisiae reveals 30 open reading frames.";
RL   Yeast 12:281-288(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=9200815;
RX   DOI=10.1002/(sici)1097-0061(19970615)13:7<655::aid-yea120>3.0.co;2-i;
RA   Voss H., Benes V., Andrade M.A., Valencia A., Rechmann S., Teodoru C.,
RA   Schwager C., Paces V., Sander C., Ansorge W.;
RT   "DNA sequencing and analysis of 130 kb from yeast chromosome XV.";
RL   Yeast 13:655-672(1997).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=9169874;
RA   Dujon B., Albermann K., Aldea M., Alexandraki D., Ansorge W., Arino J.,
RA   Benes V., Bohn C., Bolotin-Fukuhara M., Bordonne R., Boyer J., Camasses A.,
RA   Casamayor A., Casas C., Cheret G., Cziepluch C., Daignan-Fornier B.,
RA   Dang V.-D., de Haan M., Delius H., Durand P., Fairhead C., Feldmann H.,
RA   Gaillon L., Galisson F., Gamo F.-J., Gancedo C., Goffeau A., Goulding S.E.,
RA   Grivell L.A., Habbig B., Hand N.J., Hani J., Hattenhorst U., Hebling U.,
RA   Hernando Y., Herrero E., Heumann K., Hiesel R., Hilger F., Hofmann B.,
RA   Hollenberg C.P., Hughes B., Jauniaux J.-C., Kalogeropoulos A.,
RA   Katsoulou C., Kordes E., Lafuente M.J., Landt O., Louis E.J., Maarse A.C.,
RA   Madania A., Mannhaupt G., Marck C., Martin R.P., Mewes H.-W., Michaux G.,
RA   Paces V., Parle-McDermott A.G., Pearson B.M., Perrin A., Pettersson B.,
RA   Poch O., Pohl T.M., Poirey R., Portetelle D., Pujol A., Purnelle B.,
RA   Ramezani Rad M., Rechmann S., Schwager C., Schweizer M., Sor F., Sterky F.,
RA   Tarassov I.A., Teodoru C., Tettelin H., Thierry A., Tobiasch E.,
RA   Tzermia M., Uhlen M., Unseld M., Valens M., Vandenbol M., Vetter I.,
RA   Vlcek C., Voet M., Volckaert G., Voss H., Wambutt R., Wedler H.,
RA   Wiemann S., Winsor B., Wolfe K.H., Zollner A., Zumstein E., Kleine K.;
RT   "The nucleotide sequence of Saccharomyces cerevisiae chromosome XV.";
RL   Nature 387:98-102(1997).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=ATCC 204508 / S288c;
RX   PubMed=24374639; DOI=10.1534/g3.113.008995;
RA   Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA   Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA   Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT   "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL   G3 (Bethesda) 4:389-398(2014).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-157.
RC   STRAIN=ATCC 28383 / FL100 / VTT C-80102;
RX   PubMed=8798783; DOI=10.1074/jbc.271.40.25011;
RA   Crabeel M., Soetens O., de Rijcke M., Pratiwi R., Pankiewicz R.;
RT   "The ARG11 gene of Saccharomyces cerevisiae encodes a mitochondrial
RT   integral membrane protein required for arginine biosynthesis.";
RL   J. Biol. Chem. 271:25011-25018(1996).
RN   [6]
RP   SUBCELLULAR LOCATION, INTERACTION WITH CNM67, AND INDUCTION.
RX   PubMed=14515169;
RA   Wysocka M., Bialkowska A., Micialkiewicz A., Kurlandzka A.;
RT   "YOR129c, a new element interacting with Cnm67p, a component of the spindle
RT   pole body of Saccharomyces cerevisiae.";
RL   Acta Biochim. Pol. 50:883-890(2003).
RN   [7]
RP   LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX   PubMed=14562106; DOI=10.1038/nature02046;
RA   Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA   O'Shea E.K., Weissman J.S.;
RT   "Global analysis of protein expression in yeast.";
RL   Nature 425:737-741(2003).
RN   [8]
RP   FUNCTION, INTERACTION WITH ARF3, INDUCTION, SUBCELLULAR LOCATION, AND
RP   MUTAGENESIS OF 38-LYS--PRO-41.
RX   PubMed=18397879; DOI=10.1074/jbc.m802550200;
RA   Tsai P.-C., Lee S.-W., Liu Y.-W., Chu C.-W., Chen K.-Y., Ho J.-C.,
RA   Lee F.-J.;
RT   "Afi1p functions as an Arf3p polarization-specific docking factor for
RT   development of polarity.";
RL   J. Biol. Chem. 283:16915-16927(2008).
CC   -!- FUNCTION: Involved in actin patch polarization. Required for
CC       maintaining a proper budding pattern in yeast cells. Required for
CC       proper polarized localization of the ADP-ribosylation factor ARF3 at
CC       the plasma membrane. {ECO:0000269|PubMed:18397879}.
CC   -!- SUBUNIT: Interacts with ARF3 (in GTP-bound form). Interacts with CNM67.
CC       {ECO:0000269|PubMed:14515169, ECO:0000269|PubMed:18397879}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm, perinuclear region. Cytoplasm, cell
CC       cortex. Note=Enriched at the nuclear envelope and at the plasma
CC       membrane, especially in daughter cells and at the bud neck.
CC   -!- INDUCTION: Mainly expressed in dividing cells, but not in stationary
CC       phase cells (at protein level). {ECO:0000269|PubMed:14515169,
CC       ECO:0000269|PubMed:18397879}.
CC   -!- MISCELLANEOUS: Present with 768 molecules/cell in log phase SD medium.
CC       {ECO:0000269|PubMed:14562106}.
CC   -!- SIMILARITY: Belongs to the AFI1/mesA family. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAA60863.1; Type=Frameshift; Evidence={ECO:0000305};
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DR   EMBL; X90518; CAA62121.1; -; Genomic_DNA.
DR   EMBL; X94335; CAA64048.1; -; Genomic_DNA.
DR   EMBL; Z75037; CAA99328.1; -; Genomic_DNA.
DR   EMBL; X87414; CAA60863.1; ALT_FRAME; Genomic_DNA.
DR   EMBL; BK006948; DAA10903.1; -; Genomic_DNA.
DR   PIR; S61000; S61000.
DR   RefSeq; NP_014772.1; NM_001183548.1.
DR   AlphaFoldDB; Q99222; -.
DR   BioGRID; 34524; 64.
DR   IntAct; Q99222; 2.
DR   MINT; Q99222; -.
DR   STRING; 4932.YOR129C; -.
DR   iPTMnet; Q99222; -.
DR   MaxQB; Q99222; -.
DR   PaxDb; Q99222; -.
DR   PRIDE; Q99222; -.
DR   EnsemblFungi; YOR129C_mRNA; YOR129C; YOR129C.
DR   GeneID; 854296; -.
DR   KEGG; sce:YOR129C; -.
DR   SGD; S000005655; AFI1.
DR   VEuPathDB; FungiDB:YOR129C; -.
DR   eggNOG; ENOG502QQUZ; Eukaryota.
DR   HOGENOM; CLU_324667_0_0_1; -.
DR   InParanoid; Q99222; -.
DR   OMA; YIISAEF; -.
DR   BioCyc; YEAST:G3O-33653-MON; -.
DR   PRO; PR:Q99222; -.
DR   Proteomes; UP000002311; Chromosome XV.
DR   RNAct; Q99222; protein.
DR   GO; GO:0005938; C:cell cortex; IEA:UniProtKB-SubCell.
DR   GO; GO:0005935; C:cellular bud neck; IDA:SGD.
DR   GO; GO:0005737; C:cytoplasm; HDA:SGD.
DR   GO; GO:0005634; C:nucleus; IMP:SGD.
DR   GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IDA:SGD.
DR   GO; GO:0051666; P:actin cortical patch localization; IMP:SGD.
DR   GO; GO:0000282; P:cellular bud site selection; IMP:SGD.
DR   InterPro; IPR012860; Afi1_N.
DR   InterPro; IPR037516; Tripartite_DENN.
DR   Pfam; PF07792; Afi1; 1.
DR   PROSITE; PS50211; DENN; 1.
PE   1: Evidence at protein level;
KW   Coiled coil; Cytoplasm; Reference proteome.
FT   CHAIN           1..893
FT                   /note="ARF3-interacting protein 1"
FT                   /id="PRO_0000066256"
FT   DOMAIN          28..335
FT                   /note="uDENN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT   DOMAIN          365..492
FT                   /note="cDENN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT   DOMAIN          494..640
FT                   /note="dDENN"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00304"
FT   REGION          25..488
FT                   /note="Interaction with active ARF3"
FT   REGION          841..893
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          152..172
FT                   /evidence="ECO:0000255"
FT   COILED          872..892
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        843..885
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MUTAGEN         38..41
FT                   /note="KLGP->AAAA: Abolishes interaction with ARF3."
FT                   /evidence="ECO:0000269|PubMed:18397879"
SQ   SEQUENCE   893 AA;  102250 MW;  EFAEBE618FBDD989 CRC64;
     MLRRELNNSI SNRSIENESF PFERPNVSYI ISAEFDNKLG PILKHQYPKD IPGFNQFSHE
     QRNGNTSVSM NLASLMIPSS IERNPGKQDI TVFTLYYNKF TQNYQLFPVP KDPRFSFNLH
     HREQSDGSVT NSIYYDAENH QDAKNNRYTI VLEDDELECQ EVQNNQKAID NEPLFFINVA
     NTVLDTTNDR GAVIKSIAIG TPLKTFFAFK NIIVLVLDLY MKAPTQAAAT DILLDCFNML
     NSIDLTLIND IHSKSSIQEV LHSIHDESII TKVFLDPDST LKKLFCINGF DTKDKYGNIV
     TFHDQLIQYH FTRFQPKTLP PFLLKIPLQF NMIRREPIYI ENDYNELVLK FLDKFVPYLL
     KAGQKVNAWK LVINSTKLSK EDLCAFILSL ANITATYASD PQSYFKGNAA LIFPYMDISL
     VDGLRAYVAS NSDFVGCFAI IGTANPIFRY QLDIWDYYYD VDEGVFYENN SPEKEKPDTV
     AEVKIGPNPL RKIFNRPHFS TNAVNESQVN LGQKLFSLLI DEYHDSDTIM SVLRRLNVLQ
     LENLLDALKR REIPPNIALK DEYIMFYKDF FIFPEFFDYF TLHSIELLSN LDNCLFSLGN
     TCQLFSTEQI YSQLSQILDI VKELFRMVSV SRTNIEKFLN ACLNYSPFKI LPTAQLHGDN
     ISRWSFESEV RQGFDNFNSY MGIEKDPHGV IVSAIDLFTQ IYSFDILAFF LTFITKESGQ
     DLPFTKSLSR RRTYLTRIAQ SSSLRQFLQL STRPNIRILG GNGQGTGNSN YPEFTNASSV
     ISPKLRASPL LERRASKICY AITKLLYRLE CHPIGMALLK KYLHNQLREA YLESKRHFIS
     KKGDSTNTSS TIASSSFAGA SVPLSSNESG MLNGLKQINE QQESTLETTQ KED